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Conserved domains on  [gi|713693808|ref|NP_001289686|]
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putative transcription factor ovo-like protein 3 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10603440)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
SCOP:  4003583

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
112-137 3.35e-06

Zinc-finger double domain;


:

Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-06
                          10        20
                  ....*....|....*....|....*.
gi 713693808  112 DLKRHMRTHTGIRPFRCSACGKAFTQ 137
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA super family cl49620
Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, ...
126-150 9.33e-03

Kinetoplastid RNA Editing Protein A (KREPA); The KREPA 1-6 (TbMP81, 63, 42, 24, 19, and 18, respectively) proteins are components of the RNA editing complex of parasitic protozoans such as Trypanosoma and Leishmania species. These parasites have a uniquely organized mitochondrial genome, the kinetoplast. Most kinetoplast-transcribed mRNAs are cryptic and encode multiple subunits for the electron transport chain following maturation through a uridine insertion/deletion process called RNA editing. KREPAs participate in the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. The editosome, a high molecular mass enzyme complex, carries out the reaction with the help of critical enzymes and structural proteins. Five related editosome proteins KREPA1 (TbMP81), KREPA2 (TbMP63), KREPA3 (TbMP42), KREPA4 (TbMP24), KREPA5 (TbMP19), and KREPA6 (TbMP18) play critical roles in the structure and auxiliary functions of the editing process without any predicted catalytic function. The KREPA1, KREPA2, and KREPA3 proteins contain C2H2 zinc finger motifs and KREPA4 and KREPA6, contain RNA-binding domains but all have a conserved C-terminal sequences that resemble an oligonucleotide-binding (OB)-fold domain. Thus, this group of five proteins is likely to be involved in protein-protein and/or protein-RNA interactions. RNA editing is crucial for the parasite's survival in both its bloodstream and procyclic form life cycle stages which allows the parasite to adapt to its environment and maintain its viability.


The actual alignment was detected with superfamily member cd23512:

Pssm-ID: 483960  Cd Length: 449  Bit Score: 35.91  E-value: 9.33e-03
                         10        20
                 ....*....|....*....|....*
gi 713693808 126 FRCSACGKAFTQRCSLEAHLAKVHG 150
Cdd:cd23512   99 FHCSACGKAFRLRFSAEHHVKLRHP 123
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
112-137 3.35e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-06
                          10        20
                  ....*....|....*....|....*.
gi 713693808  112 DLKRHMRTHTGIRPFRCSACGKAFTQ 137
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
126-150 9.33e-03

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 35.91  E-value: 9.33e-03
                         10        20
                 ....*....|....*....|....*
gi 713693808 126 FRCSACGKAFTQRCSLEAHLAKVHG 150
Cdd:cd23512   99 FHCSACGKAFRLRFSAEHHVKLRHP 123
 
Name Accession Description Interval E-value
zf-H2C2_2 pfam13465
Zinc-finger double domain;
112-137 3.35e-06

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 41.97  E-value: 3.35e-06
                          10        20
                  ....*....|....*....|....*.
gi 713693808  112 DLKRHMRTHTGIRPFRCSACGKAFTQ 137
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPECGKSFKS 26
KREPA1 cd23512
Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial ...
126-150 9.33e-03

Kinetoplastid RNA Editing Protein A1 (KREPA1); The KREPA1 (TbMP81) protein is a crucial component of the parasitic protozoan's KREPA RNA editing complex. Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. However, the C-terminal zinc-finger domain in KREPA1 has additional amino acids. KREPA1 is involved in the insertion sub-complex of editing activities and interacts with KREPA6 of the 20S editosome core complex. When KREPA1 is down-regulated, insertion editing is preferentially inhibited.


Pssm-ID: 467777  Cd Length: 449  Bit Score: 35.91  E-value: 9.33e-03
                         10        20
                 ....*....|....*....|....*
gi 713693808 126 FRCSACGKAFTQRCSLEAHLAKVHG 150
Cdd:cd23512   99 FHCSACGKAFRLRFSAEHHVKLRHP 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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